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Literature summary for 3.1.3.48 extracted from

  • Leitherer, S.; Clos, J.; Liebler-Tenorio, E.M.; Schleicher, U.; Bogdan, C.; Soulat, D.
    Characterization of the protein tyrosine phosphatase LmPRL-1 secreted by Leishmania major via the exosome pathway (2017), Infect. Immun., 85, e00084-17 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.3.48

Cloned(Commentary)

Cloned (Comment) Organism
gene PRL-1, the gene is located on chromosome 16, sequence comparisons and phylogenetic analysis, recombinant expression of His6-LmPRL-1 in Escherichia coli, recombinant ectopical expression of hemagglutinin (HA3)-tagged LmPRL-1 in Leishmania major parasites, HA3-tagged LmPRL-1 is secreted by Leishmania major promastigotes inside exosomes Leishmania major

Protein Variants

Protein Variants Comment Organism
C172S site-directed mutagenesis Leishmania major

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00932
-
 4-nitrophenyl phosphate pH 6.0, 37°C, recombinant His-tagged enzyme Leishmania major

Localization

Localization Comment Organism GeneOntology No. Textmining
exosome
-
 Leishmania major
-
-
extracellular the enzyme secreted Leishmania major
-
-
additional information subcellular localization of LmPRL-1 in Leishmania major promastigotes depends on its C-terminal farnesylation Leishmania major
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[a protein]-tyrosine phosphate + H2O Leishmania major
-
 [a protein]-tyrosine + phosphate
-
 ?
[a protein]-tyrosine phosphate + H2O Leishmania major MHOM/IL/81/FEBNI
-
 [a protein]-tyrosine + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Leishmania major Q4QEZ7
-
-
Leishmania major MHOM/IL/81/FEBNI Q4QEZ7
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information subcellular localization of LmPRL-1 in Leishmania major promastigotes depends on its C-terminal farnesylation Leishmania major

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-LmPRL-1 from Escherichia coli by nickel affinity chromatography Leishmania major

Source Tissue

Source Tissue Comment Organism Textmining
amastigote
-
 Leishmania major
-
additional information the phosphatase is predominantly expressed and secreted by promastigotes via the exosome route. Ectopic expression of LmPRL-1 in Leishmania major leads to an increased number of parasites in host macrophages Leishmania major
-
promastigote
-
 Leishmania major
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl phosphate + H2O
-
 Leishmania major 4-nitrophenol + phosphate
-
 ?
4-nitrophenyl phosphate + H2O
-
 Leishmania major MHOM/IL/81/FEBNI 4-nitrophenol + phosphate
-
 ?
additional information strict specificity of Spd1837 for phosphotyrosine residues Leishmania major ?
-
 ?
additional information strict specificity of Spd1837 for phosphotyrosine residues Leishmania major MHOM/IL/81/FEBNI ?
-
 ?
[a protein]-tyrosine phosphate + H2O
-
 Leishmania major [a protein]-tyrosine + phosphate
-
 ?
[a protein]-tyrosine phosphate + H2O
-
 Leishmania major MHOM/IL/81/FEBNI [a protein]-tyrosine + phosphate
-
 ?

Subunits

Subunits Comment Organism
More the structures of the protein consists of alpha-helices surrounding a five-stranded beta-sheet, which represents the canonical structure of tyrosine phosphatases Leishmania major

Synonyms

Synonyms Comment Organism
LMJF_16_0230
-
 Leishmania major
LmPRL-1
-
 Leishmania major
PRL-1
-
 Leishmania major
protein tyrosine phosphatase
-
 Leishmania major
PTP
-
 Leishmania major

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Leishmania major

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 recombinant enzyme Leishmania major

General Information

General Information Comment Organism
evolution the Leishmania major phosphatase LmPRL-1 is a homologue of the human PRLs Leishmania major
physiological function the parasite enzyme LmPRL-1 shows a strong structural similarity to the human phosphatases of regenerating liver, PRL-1, -2, and -3, that regulate the proliferation, differentiation, and motility of cells Leishmania major